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- Publications
- Influence
Structure and physiological function of calpains.
- H. Sorimachi, S. Ishiura, K. Suzuki
- Biology, Medicine
- The Biochemical journal
- 15 December 1997
For a long time now, two ubiquitously expressed mammalian calpain isoenzymes have been used to explore the structure and function of calpain. Although these two calpains, mu- and m-calpains, still… Expand
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.
- S. Strobl, C. Fernández-Catalán, +9 authors W. Bode
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences…
- 18 January 2000
Calpains (calcium-dependent cytoplasmic cysteine proteinases) are implicated in processes such as cytoskeleton remodeling and signal transduction. The 2.3-A crystal structure of full-length… Expand
Calpain: new perspectives in molecular diversity and physiological‐pathological involvement
- T. Saido, H. Sorimachi, K. Suzuki
- Biology, Medicine
- FASEB journal : official publication of the…
- 1 August 1994
Calpain, calcium‐activated neutral protease, stands as a unique receptor for calcium signals in biological systems; its activation leads to irreversible proteolytic processing of substrate proteins,… Expand
Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain.
- T. Centner, J. Yano, +9 authors S. Labeit
- Biology, Medicine
- Journal of molecular biology
- 2 March 2001
The giant myofibrillar protein titin contains within its C-terminal region a serine-threonine kinase of unknown function. We have identified a novel muscle specific RING finger protein, referred to… Expand
Myopalladin, a Novel 145-Kilodalton Sarcomeric Protein with Multiple Roles in Z-Disc and I-Band Protein Assemblies
- Marie-Louise Bang, Ryan E. Mudry, +7 authors S. Labeit
- Biology, Medicine
- The Journal of cell biology
- 16 April 2001
We describe here a novel sarcomeric 145-kD protein, myopalladin, which tethers together the COOH-terminal Src homology 3 domains of nebulin and nebulette with the EF hand motifs of α-actinin in… Expand
Tissue-specific expression and alpha-actinin binding properties of the Z-disc titin: implications for the nature of vertebrate Z-discs.
- H. Sorimachi, A. Freiburg, +7 authors S. Labeit
- Biology, Medicine
- Journal of molecular biology
- 1 August 1997
Titins are giant filamentous proteins which connect Z-discs and M-lines in the sarcomeres of vertebrate striated muscles. Comparison of the N-terminal region of titin (Z-disc region) from different… Expand
Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle.
- H. Sorimachi, S. Imajoh-ohmi, +4 authors K. Suzuki
- Biology, Medicine
- The Journal of biological chemistry
- 25 November 1989
Two types of calcium-dependent protease with distinct calcium requirements (termed muCANP and mCANP) are known in mammalian tissues. These two isozymes consist of different large (80-kDa) subunits… Expand
Calpains: an elaborate proteolytic system.
- Y. Ono, H. Sorimachi
- Medicine, Biology
- Biochimica et biophysica acta
- 2012
Calpain is an intracellular Ca(2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02). Recent expansion of sequence data across the species definitively shows that calpain has been… Expand
Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein.
- H. Koike, S. Tomioka, +7 authors S. Ishiura
- Chemistry, Medicine
- The Biochemical journal
- 15 October 1999
MDC9, also known as meltrin gamma, is a membrane-anchored metalloprotease. MDC9 contains several distinct protein domains: a signal sequence followed by a prodomain and a domain showing sequence… Expand
The structure of calpain.
- H. Sorimachi, K. Suzuki
- Biology, Medicine
- Journal of biochemistry
- 1 May 2001
Recent very rapid developments in genome and EST projects have identified an increasing number of gene products homologous to those that were previously identified by other methods. Calpain is no… Expand